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ARS Home » Midwest Area » West Lafayette, Indiana » Crop Production and Pest Control Research » Research » Publications at this Location » Publication #65131
Title: MICROPLATE ASSAY FOR SOYBEAN SEED COST PEROXIDASE ACTIVITY

Author
item VIERLING, R - INDIANA CROP IMPROV ASSOC
item Wilcox, James

Submitted to: Seed Science and Technology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 4/15/1996
Publication Date: N/A
Citation: N/A

Interpretive Summary: Peroxidase can serve as an alternative to bleaches and formaldehyde in several industrial processes. Soybean seed coats are a source of peroxidase and the presence of seed coat peroxidase is controlled by a single dominant gene. A non-destructive, quantitative assay was developed that detects different levels of peroxidase activity in soybean seed coats that contain this chemical. Considerable variability was found among soybean genotypes in levels of seed coat peroxidase using this technique. The technique provides the technology to rapidly screen soybean germplasm for genotypes that are high in seed coat peroxidase activity and that will be an important source of peroxidase for industry.

Technical Abstract: Soybean seed coats are an ideal source of peroxidase. Because of the oxidative nature of peroxidase, there are several areas where it could replace current chemical oxidation techniques. The objective of this research was to develop a non-destructive, quantitative peroxidase assay for efficient identification of high-peroxidase soybean genotypes. An enzyme-capture assay was developed, which allowed for both sensitive and reliable quantification of peroxidase activity. The technique showed a linear response to solutions of known peroxidase activity and can distinguish between high and low peroxidase cultivars as measured by quaiacol. The technique identified differences in peroxidase activity between genotypes within a segregating population and will aid in the efficient selection of high-peroxidase cultivars. High-peroxidase soybean cultivars can provide a large, renewable source of peroxidase.